Sandbox GGC2

From Proteopedia

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== Structure ==
== Structure ==
Glucokinase is a protein contains 465 amino acid residues which make up two domains, including a <scene name='75/752269/Small_domain__green/1'>small domain</scene> and a <scene name='75/752269/Small_domain__green/1'>large domain</scene>.
Glucokinase is a protein contains 465 amino acid residues which make up two domains, including a <scene name='75/752269/Small_domain__green/1'>small domain</scene> and a <scene name='75/752269/Small_domain__green/1'>large domain</scene>.
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When glucose molecule binds to the <scene name='75/752269/Gkactivesite_glucose/3'>active site</scene> of glucoskinase, it forms hydrogen bonds with <scene name='75/752269/Gkactivesite_glucose/2'>Asn 204, Asp 205, Asn 231, Glu 256 and Glu 290</scene>. At the allosteric site, either glucokinase activators (GKA) or glucokinase inhibitor (GKI)will bind to regulate the activity of glucokinase by changing the confirmation. JSmol structure shows an example of GK-GKA complex, where the GKA bind to the allosteric site.
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When glucose molecule binds to the <scene name='75/752269/Gkactivesite_glucose/4'>active site</scene> of glucoskinase, it forms hydrogen bonds with <scene name='75/752269/Gkactivesite_glucose/2'>Asn 204, Asp 205, Asn 231, Glu 256 and Glu 290</scene>. At the <scene name='75/752269/Gkallosteric/1'>allosteric site</scene>, either glucokinase activators (GKA) or glucokinase inhibitor (GKI) will bind to regulate the activity of glucokinase by changing the confirmation. JSmol structure shows an example of GK-GKA complex, where the GKA bind to the allosteric site.
== Function ==
== Function ==

Revision as of 03:19, 28 April 2017

Glucokinase

Caption for this structure

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References

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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